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J Biol Chem, Vol. 274, Issue 8, 4527-4531, February 19, 1999
From the Institute of Medical Microbiology and Hygiene, Medical
University of Lübeck, 23538 Lübeck, Germany
Capsid assembly is the final event of virus
replication, and its understanding is pivotal for the design of empty
capsid-based recombinant vaccines and drug delivery systems. Although
the capsid structure of several members of the picornavirus family has
been elucidated, little is known about the structural elements
governing the assembly process that is tightly associated with
proteolytic processing of the viral polyprotein. Among the
picornaviruses, hepatitis A virus (HAV) is unique in that it contains
VP1-2A as a structural component and the small structural protein VP4,
which argues for an assembly pathway different from that proposed for other picornaviruses. Using a recombinant system we show here that
proteolytic processing of the HAV capsid proteins' precursor P1-2A is
independent of the terminal domains 2A and VP4 of the substrate.
However, both terminal domains play distinct roles in the assembly of
viral particles. 2A as part of P1-2A is a primary signal for the
assembly of pentameric structures which only further aggregate to empty
viral capsids when VP4 is present as the N terminus of the precursor.
Particle formation in the hepatovirus genus is thus regulated by two
intrinsic signals that are distinct from those described for other picornaviruses.
Intrinsic Signals for the Assembly of Hepatitis A Virus
Particles
ROLE OF STRUCTURAL PROTEINS VP4 AND 2A
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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